ID D8TIE9_VOLCA Unreviewed; 1596 AA.
AC D8TIE9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=30S ribosomal protein S3, chloroplastic {ECO:0008006|Google:ProtNLM};
GN ORFNames=VOLCADRAFT_120230 {ECO:0000313|EMBL:EFJ53228.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ53228.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC {ECO:0000256|ARBA:ARBA00025673}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|RuleBase:RU003624}.
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DR EMBL; GL378323; EFJ53228.1; -; Genomic_DNA.
DR RefSeq; XP_002946233.1; XM_002946187.1.
DR STRING; 3068.D8TIE9; -.
DR GeneID; 9625500; -.
DR KEGG; vcn:VOLCADRAFT_120230; -.
DR eggNOG; KOG0387; Eukaryota.
DR eggNOG; KOG3181; Eukaryota.
DR InParanoid; D8TIE9; -.
DR OrthoDB; 5472739at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd22254; CSB_WHD; 1.
DR CDD; cd18000; DEXHc_ERCC6; 1.
DR CDD; cd02413; KH-II_40S_S3; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR001351; Ribosomal_uS3_C.
DR InterPro; IPR018280; Ribosomal_uS3_CS.
DR InterPro; IPR005703; Ribosomal_uS3_euk/arc.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR NCBIfam; TIGR01008; uS3_euk_arch; 1.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003624};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003624};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00118}.
FT DOMAIN 465..639
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 780..935
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1387..1458
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1596 AA; 170756 MW; E39358C8F6868A0D CRC64;
MSPHGQQHQQ QEGHQRPGLT LVETEKDRRI RLGLLTPFDR LAGFERKHRA AGFGSLRHLG
RPELRPEEAA ALTRSGRPVG QVIAEAGRVA LEARTSRRMA QFLEPEQLPQ QERDVRRVPQ
HFWRQAASSH SAGGTSRLRR KSTLPRANTA EARAAARAAR RAERRTVAAA AAAIGGSVAG
GDGSEGAGDG GGSDGIRRRE NERRKGGRRR EEEVGGEDEE GEREGEGQRR RRRRTTRSGQ
AAGGGEAGVH PGVAGGGGGG SGGDAEASAS VTSSAESAGE GEDHSNFSDE LADGGSSGSE
SYGGTSCSAA AADDDDEGDS EVGAAGDRGD PSSYDDSLYD DADEDFYQER LRRSRAAAAA
ASAGGGGGHG AMHSSAAAAA ASGPPRQRRR RQRQRQTAGY AHLRNGDPDE RQHEQHLGEG
PKVPAEEEEE EEEEEDVVFE GGFRVPSRLY GRLFDYQQTA VKWLWELHTQ RAGGILGDEM
GLGKTVQVIA YLAGLHHSGL YRPSLIVCPA TVLRQWMREL RSWWPPFRVV LLHESGRSPP
AAATAVRPDR PALLEVALSS PSGLVLTTYD NLRLQRDLLL RVRWGVAVLD EGHKIRNPDS
EITLVCKQLH TVHRLIMSGS PIQNRLSELW SLFDFIFPGK LGTLPVFQAQ FAVPIQVGGY
SNASSLQVTT AYKCAVVLRD LTAPYLLRRR KADVAAQLPA KMEQVLFCTL VSEQLELYRA
YLASTEVGEI LEGSRRALCG IDILRKICNH PDLLERVTAQ DAEDYGNPAR SGKLRVAERV
LTSWHTARQK ALLFCQTQQM LDILEKLVAG RGWSYHRMDG GTPVAVRPRL IDDFNTNPDV
FVFLLTTKVG GLGVNLTGAT RVMLYDPDWN PSTDIQARER AWRIGQSHSV TIYRLITAGT
IEEKIYHRQI YKSFLTNKVL RDPRQKRFFT ARDISELFVL GPEYRKGASA AAAAAAGGDG
GGGTGSLVDT ETARIFGATL DMQDALRGGG SGGGGGSGKN RKGLSSTAAA AAALRRRGER
DGEDGDGSGG GAATTAAPSG PGPGLSSRCP HQGPDGGSAQ RAGWGRSSAA GQSAAAAAGG
GAYDAGDEDE VHDGGGGAEA DESRVLRELL DGGAGIRGLV DHSKIEGAND PEVIAVHAEA
QRVAQRAAEA LRRSRLACAA ASIATPTWTG RHGRAGAPQL ATAAAAPSPP WGGGTCRTQP
AQAQPRQQQQ QQQQQQRGVE SSAALLAQIR SRQQDIRSAA AAASRGADAT AGASTSTSGR
SHGGGDCSSA GGTAAERLAG ELVSFLEEHG GLVGSEELVE AFRSRVVSEQ MPLFKQVLRQ
VAGLRRRAGG GEWVLKPAFA TARVPAGLGG GEVASGVAQA QNLLAKMAVQ ISKKRKFVAD
GVFYAELNEL LTRELAEDGY SGVEVRVTPM RTEIIIRATR TQNVLGEKGR RIRELTSVVQ
KRFNFPADSV ELYAEKVLDR GLCAVAQAES LRYKLLGGLA VRRACYGVLR FVMESGAKGC
EVIVSGKLRA ARAKSMKFKD GYMVSSGNPA KVYIDAAVRH VLLRQGVLGI KVKIMKDWDP
TGKRGPRTPL PDVVKVLEPK EEEIFQEKPH IGKEDM
//
